title: Purification and partial characterization of a novel β-1,3-endoglucanase from Streptomyces rutgersensis.
abstract: A β-1,3-endoglucanase produced by Streptomyces rutgersensis was purified to a homogeneity by the fractional precipitation with ammonium sulfate, ion exchange chromatography on Q-Sepharose and hydrophobic chromatography on Butyl Sepharose. A typical procedure provided 11.74-fold purification with 12.53 % yield. SDSPAGE of the purified protein showed one protein band. The exact molecular mass of the enzyme obtained by mass spectrometry was 41.25 kDa; the isoelectric point was between pH 4.2–4.4. The optimal β-glucanase catalytic activity was at pH 7 and 50 °C. An enzyme was only active toward glucose polymers containing β-1,3 linkages and hydrolyzed Saccharomyces cerevisiae cell wall β-glucan in an endo-like way: reaction products were different molecular size β-glucans, which were larger than glucose.
authors.affiliation: JSC, Biocentras, Graiciuno St. 10, 02241 Vilnius, Lithuania. arturas@biocentras.lt
authors.forename: Artur
authors.initials: A
authors.lastname: Javmen
authors.forename: Saulius
authors.initials: S
authors.lastname: Grigiskis
authors.forename: Mark
authors.initials: M
authors.lastname: Rudenkov
authors.forename: Mykolas
authors.initials: M
authors.lastname: Mauricas
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D002480:Cellulase / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008970:Molecular Weight; D013302:Streptomyces / Q000737:chemistry / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D002480:Cellulase